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Database: UniProt
Entry: A0A0M5KVD5_9MICC
LinkDB: A0A0M5KVD5_9MICC
Original site: A0A0M5KVD5_9MICC 
ID   A0A0M5KVD5_9MICC        Unreviewed;       522 AA.
AC   A0A0M5KVD5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   ORFNames=AL755_19625 {ECO:0000313|EMBL:ALE07166.1};
OS   Arthrobacter sp. ERGS1:01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE07166.1, ECO:0000313|Proteomes:UP000060433};
RN   [1] {ECO:0000313|EMBL:ALE07166.1, ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE07166.1,
RC   ECO:0000313|Proteomes:UP000060433};
RX   PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA   Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT   "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT   bacterium with prospective cold active industrial enzymes, isolated from
RT   East Rathong glacier in India.";
RL   J. Biotechnol. 214:139-140(2015).
RN   [2] {ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA   Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT   "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CP012479; ALE07166.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M5KVD5; -.
DR   STRING; 1704044.AL755_19625; -.
DR   KEGG; are:AL755_19625; -.
DR   PATRIC; fig|1704044.3.peg.3284; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000060433; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060433};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          7..82
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          225..262
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          93..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  52483 MW;  7C599DA850B3D31A CRC64;
     MGGLMSPQVF LLPDLGEGLV EAELVTWLVA VGDTIHVDQP IAEVETAKSV VEVPSPFEGT
     VETLHGAEGD TLEVGKPLIS VAALGSLDSD AAVPAGEAAP TPARPQALPG LASSPQVPRA
     SGPTAVPTTP WAGAAAPALG TSAPDSPLAA APEPSDAEAA AVTSPVAVSE PAASGGSGNV
     LIGYGTSSHG GPGRTRPSRR SHLLGVSGVT AAVPASAVPH RAHLVVSPLV RKMAHDNGVA
     LADIHGSGAG GLILRRDVEA AIAPVAAPGA DHADAAEAGG AGVVDPRTGL HVLARTPLTG
     VKKAAATALA RSRREIPEAT VWVDVDATAL LELRASLKAK DGTAPSILAF VARFVTAGLA
     RFPQLNTQLV SDGGTDTVVE FDGINLGFAA QTDRGLVVPV LRGAQGRSAR ALDGAIRELT
     GTARDGKAGP AQLSGGTFTI NNYGVFGVDG SAAIINYPEA AMLGIGRITD KPWVVDGQLC
     VRKLTELTLA FDHRVCDGAV AAGFLRFIAD AMENPASALA EL
//
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